Physicochemical forces which sequester cell solutes from soluble form to organized structures are investigated with regard to molecular conformations of components and interacting species. Earlier results showed that ordered, negative charges (glycosaminoglycans) have specific ordering effects on amine cations. The current project studies polyanions inducing conformational constraints in otherwise nonordered cationic polypeptides. Polysaccharides (PS) examined for conformation-promoting-effects on poly-L-lysine showed little specificity; all with sufficient anionic density promoted a high degree of alpha-helical conformation; specificity dependent upon peptide structure revealed that interactions of heparin (and other polyanions) with copolymer L-lysine:L-tyrosine promoted the Beta-protein structure, whole those with copolymer l-lysine:L-phenylalanine induce alpha-helical order. That the nature of conformational changes in protein models due to interaction with heparin depends upon constellations of amino acids and their proclivity for alpha-helix or beta-structures is significant in the molecular basis of multianion action in granule formation and enzyme activation. Currently, heparin activation of tyrosine hydroxylase and heparin isoelectric focusing have been studied on the basis of molecular characterization.